MutSα mismatch repair protein stability is governed by subunit interaction, acetylation, and ubiquitination

Tim Arlow; Junwon Kim; Joanna E. Haye-Bertolozzi; Cristina Balbás Martínez; Caitlin Fay; Emma Zorensky; Mark D. Rose; Alison E. Gammie

doi:10.1093/g3journal/jkaa065

G3: Genes, Genomes, Genetics (Jan 2021)

MutSα mismatch repair protein stability is governed by subunit interaction, acetylation, and ubiquitination

Tim Arlow,
Junwon Kim,
Joanna E. Haye-Bertolozzi,
Cristina Balbás Martínez,
Caitlin Fay,
Emma Zorensky,
Mark D. Rose,
Alison E. Gammie

Affiliations

Tim Arlow: ORCiD; Ophthalmic Associates, Johnstown, PA
Junwon Kim: Deceased
Joanna E. Haye-Bertolozzi: ORCiD; Xavier University of Louisiana, New Orleans, LA
Cristina Balbás Martínez: ORCiD; Escuelab, Madrid, Community of Madrid, Spain
Caitlin Fay: Tufts Medical Center, Boston, MA 02118
Emma Zorensky: ORCiD; Sempre Health, San Francisco, CA
Mark D. Rose: ORCiD; Georgetown University, Georgetown, Washington D.C
Alison E. Gammie: ORCiD; National Institute of General Medical Sciences, Bethesda, MD

DOI: https://doi.org/10.1093/g3journal/jkaa065
Journal volume & issue: Vol. 11, no. 3

Abstract

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AbstractIn eukaryotes, DNA mismatch recognition is accomplished by the highly conserved MutSα (Msh2/Msh6) and MutSβ (Msh2/Msh3) complexes. Previously, in the yeast Saccharomyces cerevisiaeMSH6

Published in G3: Genes, Genomes, Genetics

ISSN: 2160-1836 (Online)
Publisher: Oxford University Press
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General): Genetics
Website: https://academic.oup.com/g3journal

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